Anatomy & Physiology: The Unity of Form and Function, 7th Edition

Published by McGraw-Hill Education
ISBN 10: 0073403717
ISBN 13: 978-0-07340-371-7

Chapter 17 - Section 17.4 - Study Guide - Assess Your Learning Outcomes - Page 669: 3

Answer

Peptide hormones, including insulin, are synthesized through a multistep process within the cells of specialized endocrine glands, such as the pancreas. Insulin is a peptide hormone produced by the beta cells of the pancreatic islets of Langerhans. Here's an overview of the synthesis process of peptide hormones like insulin: 1. **Transcription and Translation:** The synthesis of peptide hormones begins with the transcription of the hormone's gene in the cell's nucleus. In the case of insulin, the insulin gene is transcribed into messenger RNA (mRNA). The mRNA is then transported from the nucleus to the cytoplasm. In the cytoplasm, ribosomes read the mRNA and synthesize the insulin precursor molecule, preproinsulin. 2. **Formation of Preproinsulin:** Preproinsulin is the initial form of the insulin precursor. It consists of three main parts: a signal peptide, the B chain of insulin, and the A chain of insulin. The signal peptide directs the nascent preproinsulin molecule to the endoplasmic reticulum (ER) for processing. 3. **Processing in the Endoplasmic Reticulum:** In the ER, the signal peptide is cleaved off, resulting in the formation of proinsulin. Proinsulin consists of the B chain, the C peptide (derived from the signal peptide), and the A chain. Proinsulin is then transported to the Golgi apparatus for further processing. 4. **Cleavage of Proinsulin:** Within the Golgi apparatus, specific enzymes cleave the C peptide from proinsulin, resulting in the formation of mature insulin. The B and A chains of insulin are linked by disulfide bonds, forming the characteristic three-dimensional structure of the hormone. 5. **Storage in Secretory Granules:** Mature insulin is packaged into secretory granules within the beta cells of the pancreas. These granules contain a mixture of insulin and a small amount of C peptide, which serves as a marker of insulin production. 6. **Release in Response to Stimuli:** When blood glucose levels rise, such as after a meal, beta cells are stimulated to release insulin. This process involves the fusion of insulin-containing secretory granules with the cell membrane, resulting in the secretion of insulin into the bloodstream. 7. **Physiological Effects:** Once in the bloodstream, insulin travels to target cells, particularly muscle, adipose tissue, and liver cells. Insulin promotes the uptake of glucose into these cells, lowers blood glucose levels, and has various other metabolic effects that help regulate energy storage and utilization. In summary, the synthesis of peptide hormones like insulin involves transcription and translation of the hormone's gene, followed by a series of processing steps in the endoplasmic reticulum and Golgi apparatus. The mature hormone is then stored in secretory granules and released in response to physiological cues to exert its effects on target tissues.

Work Step by Step

Peptide hormones, including insulin, are synthesized through a multistep process within the cells of specialized endocrine glands, such as the pancreas. Insulin is a peptide hormone produced by the beta cells of the pancreatic islets of Langerhans. Here's an overview of the synthesis process of peptide hormones like insulin: 1. **Transcription and Translation:** The synthesis of peptide hormones begins with the transcription of the hormone's gene in the cell's nucleus. In the case of insulin, the insulin gene is transcribed into messenger RNA (mRNA). The mRNA is then transported from the nucleus to the cytoplasm. In the cytoplasm, ribosomes read the mRNA and synthesize the insulin precursor molecule, preproinsulin. 2. **Formation of Preproinsulin:** Preproinsulin is the initial form of the insulin precursor. It consists of three main parts: a signal peptide, the B chain of insulin, and the A chain of insulin. The signal peptide directs the nascent preproinsulin molecule to the endoplasmic reticulum (ER) for processing. 3. **Processing in the Endoplasmic Reticulum:** In the ER, the signal peptide is cleaved off, resulting in the formation of proinsulin. Proinsulin consists of the B chain, the C peptide (derived from the signal peptide), and the A chain. Proinsulin is then transported to the Golgi apparatus for further processing. 4. **Cleavage of Proinsulin:** Within the Golgi apparatus, specific enzymes cleave the C peptide from proinsulin, resulting in the formation of mature insulin. The B and A chains of insulin are linked by disulfide bonds, forming the characteristic three-dimensional structure of the hormone. 5. **Storage in Secretory Granules:** Mature insulin is packaged into secretory granules within the beta cells of the pancreas. These granules contain a mixture of insulin and a small amount of C peptide, which serves as a marker of insulin production. 6. **Release in Response to Stimuli:** When blood glucose levels rise, such as after a meal, beta cells are stimulated to release insulin. This process involves the fusion of insulin-containing secretory granules with the cell membrane, resulting in the secretion of insulin into the bloodstream. 7. **Physiological Effects:** Once in the bloodstream, insulin travels to target cells, particularly muscle, adipose tissue, and liver cells. Insulin promotes the uptake of glucose into these cells, lowers blood glucose levels, and has various other metabolic effects that help regulate energy storage and utilization. In summary, the synthesis of peptide hormones like insulin involves transcription and translation of the hormone's gene, followed by a series of processing steps in the endoplasmic reticulum and Golgi apparatus. The mature hormone is then stored in secretory granules and released in response to physiological cues to exert its effects on target tissues.
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